Analysis of novel regulatory mechanisms of membrane proteins mediated by protein N-myristoylation
| Project/Area Number |
17K07758
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Applied biochemistry
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| Research Institution | Yamaguchi University |
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Principal Investigator |
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| Project Period (FY) |
2017-04-01 – 2020-03-31
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| Project Status |
Completed (Fiscal Year 2019)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2019: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2018: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2017: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | N-ミリストイル化 / 膜タンパク質 / 脂質修飾タンパク質 / 機能制御機構 / タンパク質N-ミリストイル化 / タンパク質脂質修飾 / 細胞小器官 / 網羅的探索 / 機能発現 / 細胞内局在 / タンパク質-タンパク質相互作用 |
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| Outline of Final Research Achievements |
Protein N-myristoylation has been recognized as a protein modification that occurs mainly on cytoplasmic proteins. In this study, protein N-myristoylation occurring on membrane proteins was investigated. As a result, it was found that many transmembrane proteins derived from diverse cellular organelles such as endoplasmic reticulum, mitochondria, autophagosome, and lipid droplet were found to be N-myristoylated. It was also revealed that protein N-myristoylation found in these transmembrane proteins play critical roles in targeting to the organelles and/or physiological functions of these membrane proteins.
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| Academic Significance and Societal Importance of the Research Achievements |
タンパク質N-ミリストイル化は、これまで細胞質タンパク質に生ずる翻訳後修飾として知られていたが、本研究により、様々な細胞小器官に存在する多様な膜上構造を有する多くの膜タンパク質に生ずることが明らかにされ、研究の学術的意義は大きい。さらにこれらのタンパク質中には癌や神経変成疾患といった疾患と直接関与するタンパク質が複数含まれていることが示され、疾患発症のメカニズムとN-ミリストイル化との関連が注目される。このことから、本研究成果は高い社会的意義を有していると考える。
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Report
(4 results)
Research Products
(32 results)
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[Journal Article] Identification and characterization of protein N-myristoylation occurring on four human mitochondrial proteins, SAMM50, TOMM40, MIC19, and MIC25.2018
Author(s)
Utsumi T, Matsuzaki K, Kiwado A, Tanikawa A, Kikkawa Y, Hosokawa T, Otsuka A, Iuchi Y, Kobuchi H, Moriya K.
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Journal Title
PLOS ONE
Volume: 13
Issue: 11
Pages: e0206355-e0206355
DOI
Related Report
Peer Reviewed / Open Access
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